2015
Viral noncoding RNAs: more surprises
Tycowski KT, Guo YE, Lee N, Moss WN, Vallery TK, Xie M, Steitz JA. Viral noncoding RNAs: more surprises. Genes & Development 2015, 29: 567-584. PMID: 25792595, PMCID: PMC4378190, DOI: 10.1101/gad.259077.115.Peer-Reviewed Original ResearchConceptsDiverse biological rolesSmall noncoding RNAsMultitude of functionsHost immune evasionEukaryotic cellsCellular transformationNoncoding RNAsHost counterpartsAnimal virusesBiological roleNcRNAsRNA virusesViral ncRNAsMechanism of actionImmune evasionViral replicationMore surprisesBiogenesisViral persistenceRNAProteinDNAVirusRegulationReplication
2012
Conservation of a Triple-Helix-Forming RNA Stability Element in Noncoding and Genomic RNAs of Diverse Viruses
Tycowski KT, Shu MD, Borah S, Shi M, Steitz JA. Conservation of a Triple-Helix-Forming RNA Stability Element in Noncoding and Genomic RNAs of Diverse Viruses. Cell Reports 2012, 2: 26-32. PMID: 22840393, PMCID: PMC3430378, DOI: 10.1016/j.celrep.2012.05.020.Peer-Reviewed Original ResearchConceptsPAN RNAKaposi's sarcoma-associated herpesvirusSarcoma-associated herpesvirusStructure-based bioinformaticsRNA decay pathwaysDiverse viral genomesRNA stability elementNuclear retention elementPositive-strand RNA virusesReporter transcriptMammalian herpesvirusesGenomic RNAStability elementDNA virusesHuman cellsTriple helix formationRNA virusesDiverse virusesViral genomeRNAAbundant expressionDecay pathwaysTriple helixRetention elementsRapid identification
1974
Cistron specificity of 30S ribosomes heterologously reconstituted with components from Escherichia coli and Bacillus stearothermophilus.
Goldberg M, Steitz J. Cistron specificity of 30S ribosomes heterologously reconstituted with components from Escherichia coli and Bacillus stearothermophilus. Biochemistry 1974, 13: 2123-9. PMID: 4597073, DOI: 10.1021/bi00707a020.Peer-Reviewed Original ResearchDirect physical evidence for secondary structure in an isolated fragment of R17 bacteriophage mRNA
Gralla J, Steitz J, Crothers D. Direct physical evidence for secondary structure in an isolated fragment of R17 bacteriophage mRNA. Nature 1974, 248: 204-208. PMID: 4819414, DOI: 10.1038/248204a0.Peer-Reviewed Original ResearchSpecific recognition of the isolated R17 replicase initiator region by R17 coat protein
STEITZ J. Specific recognition of the isolated R17 replicase initiator region by R17 coat protein. Nature 1974, 248: 223-225. PMID: 4819415, DOI: 10.1038/248223a0.Peer-Reviewed Original ResearchHigh resolution proton NMR study of an isolated fragment of R17 bacteriophage mRNA
HILBERS CW, SHULMAN RG, YAMANE T, STEITZ JA. High resolution proton NMR study of an isolated fragment of R17 bacteriophage mRNA. Nature 1974, 248: 225-226. PMID: 4819416, DOI: 10.1038/248225a0.Peer-Reviewed Original ResearchConceptsHelical regionBase pairsBase pairingWatson-Crick base pairingIsolated fragmentsSecondary structureNMR spectraModel systemNuclear magnetic resonance spectraHigh-resolution nuclear magnetic resonance spectraNucleic acidsHydrogen-bonded protonsMagnetic resonance spectraProton NMR studiesAdjacent basesLeaf modelFragmentsNH protonsNMR studiesTRNAResonance spectraHigh-resolution proton NMR studiesHelixPairingGuanine
1968
A slowly sedimenting, infective form of bacteriophage R17
Steitz J. A slowly sedimenting, infective form of bacteriophage R17. Journal Of Molecular Biology 1968, 33: 947-951. PMID: 5700427, DOI: 10.1016/0022-2836(68)90330-6.Peer-Reviewed Original Research